RPOB_SOLM1
ID RPOB_SOLM1 Reviewed; 1369 AA.
AC C4XIN9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=DNA-directed RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE Short=RNAP subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=RNA polymerase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
DE AltName: Full=Transcriptase subunit beta {ECO:0000255|HAMAP-Rule:MF_01321};
GN Name=rpoB {ECO:0000255|HAMAP-Rule:MF_01321}; OrderedLocusNames=DMR_31160;
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate +
CC RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-
CC COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395;
CC EC=2.7.7.6; Evidence={ECO:0000255|HAMAP-Rule:MF_01321};
CC -!- SUBUNIT: The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta'
CC and 1 omega subunit. When a sigma factor is associated with the core
CC the holoenzyme is formed, which can initiate transcription.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family.
CC {ECO:0000255|HAMAP-Rule:MF_01321}.
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DR EMBL; AP010904; BAH76607.1; -; Genomic_DNA.
DR RefSeq; WP_015861765.1; NC_012796.1.
DR AlphaFoldDB; C4XIN9; -.
DR SMR; C4XIN9; -.
DR STRING; 573370.DMR_31160; -.
DR PRIDE; C4XIN9; -.
DR EnsemblBacteria; BAH76607; BAH76607; DMR_31160.
DR KEGG; dma:DMR_31160; -.
DR eggNOG; COG0085; Bacteria.
DR HOGENOM; CLU_000524_4_0_7; -.
DR OMA; FMTWEGY; -.
DR Proteomes; UP000009071; Chromosome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR CDD; cd00653; RNA_pol_B_RPB2; 1.
DR Gene3D; 2.30.150.10; -; 1.
DR Gene3D; 2.40.270.10; -; 1.
DR Gene3D; 2.40.50.150; -; 1.
DR Gene3D; 3.90.1110.10; -; 1.
DR HAMAP; MF_01321; RNApol_bact_RpoB; 1.
DR InterPro; IPR042107; DNA-dir_RNA_pol_bsu_ext_1_sf.
DR InterPro; IPR019462; DNA-dir_RNA_pol_bsu_external_1.
DR InterPro; IPR015712; DNA-dir_RNA_pol_su2.
DR InterPro; IPR007120; DNA-dir_RNAP_su2_dom.
DR InterPro; IPR037033; DNA-dir_RNAP_su2_hyb_sf.
DR InterPro; IPR010243; RNA_pol_bsu_bac.
DR InterPro; IPR007121; RNA_pol_bsu_CS.
DR InterPro; IPR007644; RNA_pol_bsu_protrusion.
DR InterPro; IPR007642; RNA_pol_Rpb2_2.
DR InterPro; IPR037034; RNA_pol_Rpb2_2_sf.
DR InterPro; IPR007645; RNA_pol_Rpb2_3.
DR InterPro; IPR007641; RNA_pol_Rpb2_7.
DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold.
DR PANTHER; PTHR20856; PTHR20856; 1.
DR Pfam; PF04563; RNA_pol_Rpb2_1; 1.
DR Pfam; PF04561; RNA_pol_Rpb2_2; 2.
DR Pfam; PF04565; RNA_pol_Rpb2_3; 1.
DR Pfam; PF10385; RNA_pol_Rpb2_45; 1.
DR Pfam; PF00562; RNA_pol_Rpb2_6; 1.
DR Pfam; PF04560; RNA_pol_Rpb2_7; 1.
DR TIGRFAMs; TIGR02013; rpoB; 1.
DR PROSITE; PS01166; RNA_POL_BETA; 1.
PE 3: Inferred from homology;
KW DNA-directed RNA polymerase; Nucleotidyltransferase; Transcription;
KW Transferase.
FT CHAIN 1..1369
FT /note="DNA-directed RNA polymerase subunit beta"
FT /id="PRO_1000214475"
SQ SEQUENCE 1369 AA; 152835 MW; F10A768E14902680 CRC64;
MAQLTKNFGK IVKTLTIPHL LNLQIDSYEL FLQKDIPPTS REDAGLEGVF RSVFPIEDFN
RTASLEYVSY EIGEPKYDVP ECIAKGLTFE APLRIKVRLV VYDVDEETEN RTIRDIKEQI
IYFGTVPLMT EKGTFIINGT ERVIVNQLQR SPGIIFEHDS GKSHTSRKVL YSCRIIPMRG
SWLDFDYDHK DILYVRIDRR RKMPATILFK AMGMSRADIL RYFYEVEHFT FEPHHVFRQV
LPDFYRKEKA YSEIRDSEGK VIVAVDKPIT KRAWRLMLEA GIEKVEVDPA TLLGLFLAED
LADPATGEVM AEAGDELNAD LIEKLKDAGI VELSLLHTRG VDTSSSIRDT LALDKTIDTI
TAQVEIYRRL RPSSPPTPEI AANFFENLFR NPDYYDLSPV GRYKINARLK VDQPLDFRTL
ANDDILKAVK HLTFLKDSHG PADDIDHLGN RRVRPVGELV ENQYRIGLVR MERAIKERMS
LQEVATLMPH DLINPKPVAA VLKEFFGTSQ LSQFMDQTNP LSEVTHKRRL SALGPGGLTR
ERAGFEVRDV HTSHYGRICP IETPEGPNIG LIVSLTTHSK VNDFGFIETP YKVVKDGQLT
GETIYLDATR EIDEVIAGAN APLDENKAFI NSMVGARIRG DQVVIPREQV TLMDISPSQI
VSVSAALIPF LEHDDANRAL MGSNMQRQAV PLLRCEQPLV GTGMEGAVAK DSGSCILAEG
EGFVHYADAE RIIVCYDDPA VGTDTGSAKT YELLKHHKSN QNTCFGQVPR VLVGQRVVKG
DVLADGPGIR DGELALGKNL LVAFMPWCGY NYEDSILISE NAVKDDTFTS VHIEEFEVVA
RDTKLGPEEI TRDIPNVGEE MLKDLDDCGI IRIGARVAPD DILVGKITPK GETQLTPEEK
LLRAIFGDKA RDVKNTSLKV PPGIEGTVID VRVFNRRSGE KDDRTRQIED FELARLDTKE
GQHAAAIAAN VRRRLWPVVS GKTVFQTIKG VKKGEVLLEA NHPMTQEVLE ALPVKKLSGL
FTSKETNEAV AEVLDEYDRH IQFIKGLYDQ KREKTTEGDD LPPGVIKMVK VYVAVKRKLN
VGDKMAGRHG NKGVVSCILP IEDMPFFSHG RPVDIVLNPL GVPSRMNIGQ ILETHLGWAG
MELGRQLAEM VDSGKAMEGV RDRAKAVFDT EETTALIDGM SDDDLRDALR ALKNGIVAKT
PVFDGATEDE LWSWLKLAGL PEDGKVTLYD GRTGEAFHRP VTVGCMYILK LHHLVDEKIH
ARSTGPYSLV TQQPLGGKAQ FGGQRLGEME VWALEAYGAS YLLQEFLTVK SDDVGGRVKM
YEKIVKGDNF LEAGLPESFN VLVKELMSLG LDVDLIQDEK KIAKAPPRR
